Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.
Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus....
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-12-01
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| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1006755 |
| _version_ | 1819141383678590976 |
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| author | Carlos P Mata Daniel Luque Josué Gómez-Blanco Javier M Rodríguez José M González Nobuhiro Suzuki Said A Ghabrial José L Carrascosa Benes L Trus José R Castón |
| author_facet | Carlos P Mata Daniel Luque Josué Gómez-Blanco Javier M Rodríguez José M González Nobuhiro Suzuki Said A Ghabrial José L Carrascosa Benes L Trus José R Castón |
| author_sort | Carlos P Mata |
| collection | DOAJ |
| description | Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface. |
| first_indexed | 2024-12-22T11:53:35Z |
| format | Article |
| id | doaj.art-a684d248d6a64880960c9e1f7e29af8c |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-22T11:53:35Z |
| publishDate | 2017-12-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-a684d248d6a64880960c9e1f7e29af8c2022-12-21T18:26:55ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742017-12-011312e100675510.1371/journal.ppat.1006755Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.Carlos P MataDaniel LuqueJosué Gómez-BlancoJavier M RodríguezJosé M GonzálezNobuhiro SuzukiSaid A GhabrialJosé L CarrascosaBenes L TrusJosé R CastónUnlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.https://doi.org/10.1371/journal.ppat.1006755 |
| spellingShingle | Carlos P Mata Daniel Luque Josué Gómez-Blanco Javier M Rodríguez José M González Nobuhiro Suzuki Said A Ghabrial José L Carrascosa Benes L Trus José R Castón Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. PLoS Pathogens |
| title | Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. |
| title_full | Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. |
| title_fullStr | Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. |
| title_full_unstemmed | Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. |
| title_short | Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses. |
| title_sort | acquisition of functions on the outer capsid surface during evolution of double stranded rna fungal viruses |
| url | https://doi.org/10.1371/journal.ppat.1006755 |
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